Industrial Bio-materials Research Center, Korea Research Institute of Bioscience and Biotechnology, Yusung, Daejeon 305-600, Republic of Korea.
J Microbiol. 2011 Dec;49(6):1018-21. doi: 10.1007/s12275-011-1376-7. Epub 2011 Dec 28.
A fibrinolytic enzyme was found in a Gram-negative bacterium, Aeromonas sp. JH1. SDS-PAGE and fibrinzymography showed that it was a 36 kDa, monomeric protein. Of note, the enzyme was highly specific for fibrinogen molecules and the hydrolysis rate of fibrinogen subunits was highest for α, β, and γ chains in that order. The first 15 amino acids of N-terminal sequence were X-D-A-T-G-P-G-G-N-V-X-T-G-K-Y, which was distinguishable from other fibrinolytic enzymes. The optimum pH and temperature of the enzyme were approximately 8.0 and 40°C, respectively. Therefore, these results provide a fibrinolytic enzyme with potent thrombolytic activity from the Aeromonas genus.
在革兰氏阴性菌气单胞菌属 JH1 中发现了一种纤维蛋白溶酶。SDS-PAGE 和纤维蛋白溶酶谱分析表明，它是一种 36 kDa 的单体蛋白。值得注意的是，该酶对纤维蛋白原分子具有高度特异性，并且纤维蛋白原亚单位的水解速率按α、β和γ链的顺序最高。N 端序列的前 15 个氨基酸为 X-D-A-T-G-P-G-G-N-V-X-T-G-K-Y，与其他纤维蛋白溶酶不同。该酶的最适 pH 和温度分别约为 8.0 和 40°C。因此，这些结果提供了一种具有强溶栓活性的纤维蛋白溶酶，来自气单胞菌属。
